CH60_PORGI
ID CH60_PORGI Reviewed; 545 AA.
AC P42375;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Chaperonin GroEL {ECO:0000255|HAMAP-Rule:MF_00600};
DE EC=5.6.1.7 {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=60 kDa chaperonin {ECO:0000255|HAMAP-Rule:MF_00600};
DE AltName: Full=Chaperonin-60 {ECO:0000255|HAMAP-Rule:MF_00600};
DE Short=Cpn60 {ECO:0000255|HAMAP-Rule:MF_00600};
GN Name=groEL {ECO:0000255|HAMAP-Rule:MF_00600};
GN Synonyms=groL {ECO:0000255|HAMAP-Rule:MF_00600}, mopA;
GN OrderedLocusNames=PG_0520;
OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=242619;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7913687; DOI=10.1111/j.1574-6968.1994.tb06879.x;
RA Maeda H., Miyamoto M., Hongyou H., Kitanaka M., Nagai A., Kurihara H.,
RA Murayama Y.;
RT "Heat shock protein 60 (GroEL) from Porphyromonas gingivalis: molecular
RT cloning and sequence analysis of its gene and purification of the
RT recombinant protein.";
RL FEMS Microbiol. Lett. 119:129-135(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=381;
RX PubMed=8086460; DOI=10.1016/0167-4781(94)90265-8;
RA Hotokezaka H., Hayashida H., Ohara N., Nomaguchi H., Kobayashi K.,
RA Yamada T.;
RT "Cloning and sequencing of the groESL homologue from Porphyromonas
RT gingivalis.";
RL Biochim. Biophys. Acta 1219:175-178(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-308 / W83;
RX PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA Fraser C.M.;
RT "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT gingivalis strain W83.";
RL J. Bacteriol. 185:5591-5601(2003).
CC -!- FUNCTION: Together with its co-chaperonin GroES, plays an essential
CC role in assisting protein folding. The GroEL-GroES system forms a nano-
CC cage that allows encapsulation of the non-native substrate proteins and
CC provides a physical environment optimized to promote and accelerate
CC protein folding. {ECO:0000255|HAMAP-Rule:MF_00600}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + a folded polypeptide = ADP + phosphate + an
CC unfolded polypeptide.; EC=5.6.1.7; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00600};
CC -!- SUBUNIT: Forms a cylinder of 14 subunits composed of two heptameric
CC rings stacked back-to-back. Interacts with the co-chaperonin GroES.
CC {ECO:0000255|HAMAP-Rule:MF_00600}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00600}.
CC -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC {ECO:0000255|HAMAP-Rule:MF_00600}.
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DR EMBL; D17398; BAA04222.1; -; Genomic_DNA.
DR EMBL; D17342; BAA04161.1; -; Genomic_DNA.
DR EMBL; AE015924; AAQ65714.1; -; Genomic_DNA.
DR PIR; S47530; S47530.
DR RefSeq; WP_005875079.1; NC_002950.2.
DR AlphaFoldDB; P42375; -.
DR SMR; P42375; -.
DR STRING; 242619.PG_0520; -.
DR EnsemblBacteria; AAQ65714; AAQ65714; PG_0520.
DR KEGG; pgi:PG_0520; -.
DR eggNOG; COG0459; Bacteria.
DR HOGENOM; CLU_016503_3_0_10; -.
DR OMA; TDTDKME; -.
DR OrthoDB; 265347at2; -.
DR PHI-base; PHI:3085; -.
DR Proteomes; UP000000588; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR CDD; cd03344; GroEL; 1.
DR Gene3D; 1.10.560.10; -; 1.
DR Gene3D; 3.30.260.10; -; 1.
DR Gene3D; 3.50.7.10; -; 1.
DR HAMAP; MF_00600; CH60; 1.
DR InterPro; IPR018370; Chaperonin_Cpn60_CS.
DR InterPro; IPR001844; Cpn60/GroEL.
DR InterPro; IPR002423; Cpn60/GroEL/TCP-1.
DR InterPro; IPR027409; GroEL-like_apical_dom_sf.
DR InterPro; IPR027413; GROEL-like_equatorial_sf.
DR InterPro; IPR027410; TCP-1-like_intermed_sf.
DR Pfam; PF00118; Cpn60_TCP1; 1.
DR PRINTS; PR00298; CHAPERONIN60.
DR SUPFAM; SSF48592; SSF48592; 1.
DR SUPFAM; SSF52029; SSF52029; 1.
DR SUPFAM; SSF54849; SSF54849; 1.
DR TIGRFAMs; TIGR02348; GroEL; 1.
DR PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Cytoplasm; Isomerase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..545
FT /note="Chaperonin GroEL"
FT /id="PRO_0000063477"
FT BINDING 29..32
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 86..90
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 415
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT BINDING 495
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00600"
FT CONFLICT 23
FT /note="A -> P (in Ref. 1; BAA04222)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="G -> V (in Ref. 1; BAA04222)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="K -> N (in Ref. 1; BAA04222)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="A -> S (in Ref. 1; BAA04222)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="A -> S (in Ref. 1; BAA04222)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="D -> A (in Ref. 1; BAA04222)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="I -> N (in Ref. 1; BAA04222)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="A -> P (in Ref. 1; BAA04222)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="T -> A (in Ref. 1; BAA04222)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="K -> N (in Ref. 1; BAA04222)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="A -> T (in Ref. 1; BAA04222)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="T -> R (in Ref. 1; BAA04222)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="A -> P (in Ref. 1; BAA04222)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="A -> P (in Ref. 1; BAA04222)"
FT /evidence="ECO:0000305"
FT CONFLICT 405..406
FT /note="AA -> PP (in Ref. 1; BAA04222)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="A -> T (in Ref. 1; BAA04222)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="V -> M (in Ref. 1; BAA04222)"
FT /evidence="ECO:0000305"
FT CONFLICT 490
FT /note="T -> S (in Ref. 2; BAA04161)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 545 AA; 58094 MW; 5ACCC6A5CBCF24B5 CRC64;
MAKEIKFDME SRDLLKKGVD ALANAVKVTL GPKGRNVILS KTYGAPHITK DGVSVAKEIE
LECPFENMGA QLVKEVASKT NDDAGDGTTT ATILAQSIIG VGLKNVTAGA NPMDLKRGID
KAVKAVVTHI AGMAKEVGDD FQKIEHVAKI SANGDENIGS LIAEAMRKVK KEGVITVEEA
KGTDTTVEVV EGMQFDRGYI SPYFVTNTDK MEVQMENPFI LIYDKKISVL KEMLPILEQT
VQTGKPLLII AEDIDSEALA TLVVNRLRGS LKICAVKAPG FGDRRKAMLE DIAILTGGTV
ISEETGLKLE NATMDMLGTA EKVTVDKDNT TIVNGAGNKE GIASRITQIK AQIENTTSDY
DREKLQERLA KLAGGVAVLY VGAASEVEMK EKKDRVEDAL SATRAAIEEG TVPGGGTAYI
RAIAALEGLK GENEDETTGI EIVKRAIEEP LRQIVANAGK EGAVVVQKVK EGKDDFGYNA
RTDVFENLYT TGVIDPAKVT RVALENAASI AGMFLTTECV IADKKEDNPA APAMPGGMGG
MGGMM
